The 1-Hydroxy-2-methyl-2-(E)-butenyl-4-diphosphate-synthase (IspG-protein) catalyzes the second to last step of the mevalonate-independent biosynthesis of the isoprenoids precursors. It could be shown that the IspG-protein is an oxygen-sensitive Fe/S protein. The recombinant enzyme could be isolated anaerobically and was active with the addition of photoreduced 10-Methyl-5-deaza-isoalloxazine or by the use of flavodoxine, flavodoxine-(NADP+)-reductase and NADPH. By the cross-linking of different work methods (radiochemically, NMR- spectroscopically and UV/Vis spectroscopically) proteinchemical as well as kinetic parameters of the IspG-protein could be determined. In addition the role of a possible intermediate (2,3-Epoxy-4-hydroxy-3-methyl-butyldiphosphate) of the reaction catalyzed by the IspG-protein, could be examined. «

The 1-Hydroxy-2-methyl-2-(E)-butenyl-4-diphosphate-synthase (IspG-protein) catalyzes the second to last step of the mevalonate-independent biosynthesis of the isoprenoids precursors. It could be shown that the IspG-protein is an oxygen-sensitive Fe/S protein. The recombinant enzyme could be isolated anaerobically and was active with the addition of photoreduced 10-Methyl-5-deaza-isoalloxazine or by the use of flavodoxine, flavodoxine-(NADP+)-reductase and NADPH. By the cross-linking of different... »